Protein Interaction & Assembly
2021 Journal Articles
Liquid–liquid phase separation of Tau by self and complex coacervation
S. Najafi, Y. Lin, A. P. Longhini, X. Zhang, K. T. Delaney, K. S. Kosik, G. H. Fredrickson, J. Shea, and S. Han. Protein Science 30 (2021), 1393-1407.
https://doi.org/10.1002/pro.4101
Homo-Oligomerization of the Human Adenosine A2A Receptor is Driven by the Intrinsically Disordered C-terminus
K. D. Q. Nguyen, M. Vigers, E. Sefah, S. Seppala, J. P. Hoover, N. S. Schonenbach, B. Mertz, M. A. O'Malley, and S. Han. eLife 10 (2021), e6662.
https://doi.org/10.7554/eLife.66662
Also published in Biorxiv.
Liquid-liquid phase separation of tau driven by hydrophobic interaction facilitates fibrillization of tau
Y. Lin, Y. Fichou, A. P. Longhini, L. C. Llanes, P. Yin, G. C. Bazan, K. S. Kosik, S. Han J. Mol. Biol., 433(2) (2021), 166731
https://doi.org/10.1016/j.jmb.2020.166731. PMID: 33279579; PMCID: PMC7855949.
2020 Journal Articles
The proline-rich domain promotes Tau liquid–liquid phase separation in cells
X. Zhang, M. Vigers, J. McCarty, J. N. Rauch, G. H. Fredrickson, M. Z. Wilson, J.-E. Shea, S. Han, and K. S. Kosik J. Cell Biol., 219 (11) (2020), e202006054
https://doi.org/10.1083/jcb.202006054. PMID: 32997736; PMCID: PMC7594490.
Dehydration entropy drives liquid-liquid phase separation by molecular crowding
S. Park, R. Barnes, Y. Lin, B.-J. Jeon, S. Najafi, K. T. Delaney, G. H. Fredrickson, J.-E. Shea, D. S. Hwang, and S. Han Comm. Chem., 3 (83) (2020)
https://doi.org/10.1038/s42004-020-0328-8
Mechanisms of heparin-induced tau aggregation revealed by single nanopore
N. Giamblanco, Y. Fichou, J.-M. Janot, E. Balanzat, S. Han, and S. Balme. ACS Sens., 5 (4) (2020), 1158–1167.
https://pubs.acs.org/doi/abs/10.1021/acssensors.0c00193. PMID: 32216272.
Electrostatic Environment of Proteorhodopsin Affects the pKa of Its Buried Primary Proton Acceptor
C.-T. Han, J. Song, T. Chan, C. Pruett, and S. Han. Biophys. J., 118 (8) (2020), 1838-1849.
https://doi.org/10.1016/j.bpj.2020.02.027. PMID: 32197061; PMCID: PMC7176579.
Electrostatically driven complex coacervation and amyloid aggregation of tau are independent processes with overlapping conditions.
Y. Lin, Y. Fichou, Z. Zeng, N. Y. Hu, and S. Han. ACS Chem. Neurosci., 11 (4) (2020), 615–627.
https://doi.org/10.1021/acschemneuro.9b00627. PMID: 31971365.
Also published in BioRxiv:
https://doi.org/10.1101/702126
2020 Book Chapter
Tau Condensates
K. Kosik, S. Han Kumar,. Adv. Exp. Med. Biol., 1184 (2020), 327-339.
https://doi.org/10.1007/978-981-32-9358-8_24. PMID: 32096047.
2019 Journal Articles
Tau-cofactor complexes as building blocks of tau fibrils
Y. Fichou, Z. R. Oberholtzer, H. Ngo, C.-Y. Cheng, T. J. Keller, N. A. Eschmann, and S. Han. Front. Neurosci., 13 (2019), 1339.
https://doi.org/10.3389/fnins.2019.01339. PMID: 31920504; PMCID: PMC6923735.
Liquid-liquid phase separation and fibrillization of tau are independent processes with overlapping conditions
Y. Lin, Y. Fichou, Z. Zeng, N. Y. Hu, and S. Han. Biorxiv (2019)
https://doi.org/10.1101/702126
Protein shapes at the core of chronic traumatic encephalopathy
Y. Fichou and S. Han. Nature Struct. Mol. Biol., 26 (2019), 336-338.
https://doi.org/10.1038/s41594-019-0221-2
Proteorhodopsin Function is Primarily Mediated by Oligomerization in Different Micellar Surfactant Solutions
M. N. Idso, N. R. Baxter, S. Narayanan, E. Chang, J. M. Fisher, B. F. Chmelka, and S. Han J. Phys. Chem. B, 123 (19) (2019), 4180-4192.
https://doi.org/10.1021/acs.jpcb.9b00922. PMID: 30924654.
Narrow equilibrium window for complex coacervation of tau and RNA under cellular conditions
Y. Lin, J. McCarty, J. N. Rauch, K. T. Delaney, K. S. Kosik, G. H. Fredrickson, J.-E. Shea, S. Han. eLife, 8 (2019), e42571
https://doi.org/10.7554/eLife.42571. PMID: 30950394; PMCID: PMC6450672.
2018 Journal Articles
Cofactors are essential constituents of stable and seeding-active tau fibrils
Y. Fichou, Y. Lin, J. N. Rauch, M. Vigers, Z. Zeng, M. Srivastava, T. J. Keller, J. H. Freed, K. S. Kosik, S. Han. Proc. Nat. Acad. Sci., 115 (52) (2018), 13234-13239.
https://doi.org/10.1073/pnas.1810058115. PMID: 30538196; PMCID: PMC6310788.
Highlighted in the UC Santa Barbara Current:
http://www.news.ucsb.edu/2018/019293/three-player-game
Tuning conformation and properties of peptidomimetic backbones through dual N/Calpha-substitution
R. Kaminker, I. Kaminker, W. R. Gutekunst, Y. Luo, S. Lee, J. Niu, S. Han, C. J. Hawker. Chem. Comm., 54 (41) (2018), 5237-5240.
https://doi.org/10.1039/C8CC01356J. PMID: 29726557; PMCID: PMC6089238.
Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer’s disease filaments
Y. Fichou, M. Vigers, A. K. Goring, N. A. Eschmann, S. Han, Chem. Commun., 54 (36) (2018), 4573-4576.
https://doi.org/10.1039/C8CC01355Aa. PMID: 29664486.
2017 Journal Articles
Conformation-based assay of tau protein aggregation
Y. Fichou, N.A. Eschmann, T.J. Keller, S. Han, Methods Cell Biol., 141 (2017) 89-112.
https://doi.org/10.1016/bs.mcb.2017.06.008. PMID: 28882313.
Proton-based structural analysis of heptahelical transmembrane protein in lipid bilayers
D. Lalli, M.N. Idso, L.B. Andreas, S. Hussain, N. Baxter, S. Han, B. Chmelka, G. Pintacuda, J. Am. Chem. Soc., 139 (37) (2017) 13006-13012.
https://doi.org/10.1021/jacs.7b02969. PMID: 28724288. PMCID: PMC5741281.
Highlighted Cover Article: http://pubs.acs.org/toc/jacsat/139/37
RNA Stores Tau Reversibly in Complex Coacervates
X. Zhang, N.E. Eschmann, Y. Lin, H. Zhou, J. Rauch, I. Hernandez, E. Guzman, K.S. Kosik, S. Han, PLOS Biol., 15 (7) (2017) e2002183.
https://doi.org/10.1371/journal.pbio.2002183. PMID: 28683104. PMCID: PMC5500003
Also published in bioRxiv:
https://doi.org/10.1016/10.1101/111245
Highlighted in:
http://www.medicalnewstoday.com/releases/318265.php
http://www.news.ucsb.edu/2017/018072/biophysical-smoking-gun
Signature of an aggregation-prone conformation of tau
N.A. Eschmann, E.R. Georgieva, P. Ganguly, P.P. Borbat, M.D. Rappaport, Y. Akdogan, J.H. Freed, J.E. Shea, S. Han, Sci. Rep., 7 (2017) 1-10
https://doi.org/10.1038/srep44739. PMID: 28303942. PMCID: PMC5356194
2016 Journal Articles
Adenosine A2a receptors form distinct oligomers in protein detergent complexes
N.S. Schonenbach, M.D. Rieth, S. Han, M.A. O'Malley, FEBS Lett., 590 (2016) 3295–3306
https://doi.org/10.1002/1873-3468.12367 PMID: 27543907; PMCID: PMC5039092.
Molecular and structural basis of low interfacial energy of complex coacervates in water
Y. Jho, H. Yoo, Y. Lin, S. Han, D. Hwang, Adv. Colloid Interface Sci., 239 (2017) 61–73
https://doi.org/10.1016/j.cis.2016.07.003. PMID: 27499328.
Biocontinuous Fluid Structure with Low Cohesive Energy: Molecular Basis for Exceptionally Low Interfacial Tension of Complex Coacervate Fluids
K. Huang, H. Yoo, Y. Jho, S. Han, D. Hwang, ACS Nano, 10 (2016) 5051-5062
https://doi.org/10.1021/acsnano.5b07787
Protein structural and surface water rearrangement constitute major events in the earliest aggregation stages of tau
A. Pavlova, C. Cheng, M. Kinnebrew, J. Lew, F. Dahlquist, S. Han, Proc. Natl. Acad. Sci., 113 (2) (2016) E127-E136
https://doi.org/10.1073/pnas.1504415113. PMID: 26712030; PMCID: PMC4720316
2015 Journal Articles
Tau Aggregation Propensity Engrained in Its Solution State
N. Eschmann, T. Do, N. LaPointe, J. Shea, S. Feinstein, M. Bowers, S. Han, J. Phys. Chem., 119 (45) (2015) 14421–14432
https://doi.org/10.1021/acs.jpcb.5b08092 PMID: 26484390; PMCID: PMC4645975
Mussel Coating Protein-Derived Complex Coacervates Mitigate Frictional Surface Damage
D. Miller, S. Das, K. Huang, S. Han, J. Israelachvili, J. Waite, ACS Biomater. Sci. Eng., 1 (11) (2015) 1121–1128
https://doi.org/10.1021/acsbiomaterials.5b00252 PMID: 26618194; PMCID: PMC4642218
ACS Editors' Choice Paper
Functional Consequences of the Oligomeric Assembly of Proteorhodopsin
S. Hussain, M. Kinnebrew, N. Schonenbach, E. Aye, S. Han, J. Molec. Biol., 427 (6B) (2015) 1278-1290
https://doi.org/10.1016/j.jmb.2015.01.004 PMID: 25597999; PMCID: PMC4374980
2014 Journal Articles
Determining the oligomeric structure of proteorhodopsin by Gd3+-based pulsed dipolar spectroscopy of multiple distances
D.T. Edwards, T. Huber, S. Hussain, K.M. Stone, M. Kinnebrew, I. Kaminker, E. Matalon, M.S. Sherwin, D. Goldfarb, S. Han, Structure, 22 (11) (2014) 1677-1686
https://doi.org/10.1016/j.str.2014.09.008 PMID: 25438671.
2013 Journal Articles
Structural Insight into Proteorhodopsin Oligomers
K. M. Stone, J. Voska, M. Kinnebrew, A. Pavlova, M. J. N. Junk, S. Han, Biophys. J., 104(2) (2013) 472-481
https://doi.org/10.1016/j.bpj.2012.11.3831 PMID: 23442869; PMCID: PMC3552253
Transmembrane Protein Activation Refined by Site-Specific Hydration Dynamics
S. Hussain, J. M. Franck, S. Han, Angew. Chem. Int. Ed., 52(7) (2013) 1953-1958
https://doi.org/10.1002/anie.201206147 PMID: 23307344
2013 Journal Articles
Annual Review of Physical Chemistry
Vol. 64, Annual Reviews (2013)
Dynamic Nuclear Polarization Methods in Solids and Solutions to Explore Membrane Proteins and Membrane Systems
C. Cheng and S. Han
https://doi.org/10.1146/annurev-physchem-040412-110028 PMID: 23331309
2007–2010 Journal Article
Site-specific Dynamic Nuclear Polarization of Hydration Water as a Generally Applicable Approach to Monitor Protein Aggregation
A. Pavlova, E.R. McCarney, D.W. Peterson, F.W. Dahlquist, J. Lew, S. Han, Phys. Chem. Chem. Phys. (PCCP) 11 (2009) 6833-6839
https://doi.org/10.1039/b906101k PMID: 19639158; PMCID: PMC3153360
